Plant aspartic proteinases: Enzymes on the way to a function

Asuman Mutlu, Susannah Gal

Research output: Contribution to journalArticle

99 Citations (Scopus)

Abstract

Plant aspartic proteinases have been characterized from seeds, flowers and leaves of a number of different species. The enzymes are generally either monomeric or heterodimeric, containing two peptides processed from the same precursor protein. The plant enzymes, like their mammalian and microbial counterparts, are active at acidic pH and inhibited by a class specific inhibitor pepstatin A. Plant aspartic proteinases are generally either secreted or targeted to the vacuolar/protein storage body compartment. The primary sequences of many of these enzymes have been determined and are very homologous with each other as well as with enzymes from mammalian and microbial origins. Plant aspartic proteinases, however, have a very unique plant specific region, which is not found in mammalian, microbial, or viral aspartic proteinases. The function of this region has not been elucidated. A role for these plant enzymes in protein processing or degradation has been proposed, however, more studies are required to confirm their in vivo functions. Recent intriguing results suggest possible roles for these enzymes in programmed cell-death of tissues and in pathogen resistance.

Original languageEnglish (US)
Pages (from-to)569-576
Number of pages8
JournalPhysiologia Plantarum
Volume105
Issue number3
DOIs
StatePublished - Mar 1 1999

Fingerprint

Aspartic Acid Proteases
aspartic proteinases
Enzymes
enzymes
Protein Precursors
Cotyledon
storage proteins
Proteins
Cell Death
apoptosis
proteins
peptides
flowers
Peptides
degradation
pathogens
seeds
leaves

All Science Journal Classification (ASJC) codes

  • Physiology
  • Genetics
  • Plant Science
  • Cell Biology

Cite this

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Plant aspartic proteinases : Enzymes on the way to a function. / Mutlu, Asuman; Gal, Susannah.

In: Physiologia Plantarum, Vol. 105, No. 3, 01.03.1999, p. 569-576.

Research output: Contribution to journalArticle

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